Crystal structure of two CD46 domains reveals an extended measles virus-binding surface

EMBO Journal

Volumn 18, Issue 11, 1999, Pages 2911-2922

  Casasnovas, José M ^a   Larvie, Mykol ^b   Stehle, Thilo ^c  

^a KAROLINSKA INSTITUTE   (Sweden)

^b HARVARD MIT DIVISION OF HEALTH SCIENCES AND TECHNOLOGY   (United States)

^c MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

CD46; Measles virus; Membrane cofactor protein; Short consensus repeat; Virus receptor interaction

Indexed keywords

AMINO ACID; ANTIVIRUS AGENT; CELL SURFACE RECEPTOR; EPITOPE; MEMBRANE COFACTOR PROTEIN;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; HUMAN; MEASLES; MEASLES VIRUS; PARAMYXOVIRUS; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANTIGENS, CD; ANTIGENS, CD4; ANTIGENS, CD46; BINDING SITES; CONSENSUS SEQUENCE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; GLYCOSYLATION; HUMANS; INTERCELLULAR ADHESION MOLECULE-1; MEASLES VIRUS; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, VIRUS; REPETITIVE SEQUENCES, AMINO ACID;

MEASLES VIRUS; PARAMYXOVIRIDAE; RESPIRATORY SYNCYTIAL VIRUS; RNA VIRUSES; SYNCYTIAL VIRUS;

EID: 0033151839     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.11.2911     Document Type: Article

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